Activation of dioxygen at a histidine- and carboxylate-ligated non-heme diiron cofactor is the <i>modus</i> <i>operandi</i> of a large and growing family of enzymes. Classic studies on soluble methane monooxygenase, class I-a ribonucleotide reductase, and stearoyl-acyl carrier protein delta-9 desaturase led to a functional paradigm for these enzymes involving formation of an initial diiron(III/III)-peroxide complex, conversion of this complex to a high-valent intermediate, and initiation of a one- or two-electron-oxidation outcome by the high-valent complex. More recent studies on newly discovered members of the class have revealed cases for which the peroxide-level complexes themselves, rather than high-valent successors, are the substrate-transforming intermediates and they effect zero- and four-electron-oxidations. This lecture will summarize what we have learned about the mechanisms of one or more of these novel non-heme-diiron oxygenases that mediate non-canonical reactions.

Novel outcomes and mechanisms emerging from dioxygen activation by non-heme-di-iron enzymes

253rd National Meeting (2017)

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